메뉴 건너뛰기




Volumn 48, Issue 32, 2009, Pages 7629-7635

A novel β-defensin structure: Big defensin changes its N-terminal structure to associate with the target membrane

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ANTI-MICROBIAL ACTIVITY; C-TERMINAL DOMAINS; DEFENSINS; GLOBULAR CONFORMATIONS; HELIX STRUCTURES; HORSESHOE CRAB; HYDROPHOBIC DOMAINS; MICELLAR ENVIRONMENT; MICELLAR SOLUTION; N-TERMINAL DOMAINS; N-TERMINALS; NMR SPECTRUM; PARAMAGNETIC PROBES;

EID: 68849090173     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900756y     Document Type: Article
Times cited : (17)

References (36)
  • 1
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: From invertebrates to vertebrates
    • Bulet, P., Stöklin, R., and Menin, L. (2004) Anti-microbial peptides: From invertebrates to vertebrates. Immunol. Rev. 198, 169-184.
    • (2004) Immunol. Rev , vol.198 , pp. 169-184
    • Bulet, P.1    Stöklin, R.2    Menin, L.3
  • 2
    • 33646532402 scopus 로고    scopus 로고
    • Host defense peptides from invertebrates: Emerging antimicrobial strategies
    • Hancock, R. E. W., Brown, K. L., and Mookherjee, N. (2006) Host defense peptides from invertebrates: Emerging antimicrobial strategies. Immunobiology 211, 315-322.
    • (2006) Immunobiology , vol.211 , pp. 315-322
    • Hancock, R.E.W.1    Brown, K.L.2    Mookherjee, N.3
  • 3
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • Ganz, T. (2003) Defensins: Antimicrobial peptides of innate immunity. Nat. Rev. Immunol. 3, 710-720.
    • (2003) Nat. Rev. Immunol , vol.3 , pp. 710-720
    • Ganz, T.1
  • 4
    • 20644462344 scopus 로고    scopus 로고
    • Mammalian defensins in the antimicrobial immune response
    • Selsted, M. E., and Ouellette, A. J. (2005) Mammalian defensins in the antimicrobial immune response. Nat. Immunol. 6, 551-557.
    • (2005) Nat. Immunol , vol.6 , pp. 551-557
    • Selsted, M.E.1    Ouellette, A.J.2
  • 5
    • 0032718949 scopus 로고    scopus 로고
    • Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systems
    • Lohner, K., and Prenner, E. J. (1999) Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systems. Biochim. Biophys. Acta 1462, 141-156.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 141-156
    • Lohner, K.1    Prenner, E.J.2
  • 6
    • 0025021992 scopus 로고
    • Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes
    • Kagan, B. L., Selsted, M. E., Ganz, T., and Lehner, R. I. (1990) Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes. Proc. Natl. Acad. Sci. U.S.A. 87, 210-214.
    • (1990) Proc. Natl. Acad. Sci. U.S.A , vol.87 , pp. 210-214
    • Kagan, B.L.1    Selsted, M.E.2    Ganz, T.3    Lehner, R.I.4
  • 7
    • 0027218376 scopus 로고
    • Defensins promote fusion and lysis of negatively charged membranes
    • Fujii, G., Selsted, M. E., and Eisenberg, D. (1993) Defensins promote fusion and lysis of negatively charged membranes. Protein Sci. 2, 1301-1312.
    • (1993) Protein Sci , vol.2 , pp. 1301-1312
    • Fujii, G.1    Selsted, M.E.2    Eisenberg, D.3
  • 8
    • 0028061984 scopus 로고
    • Interactions between human defensins and lipid bilayers: Evidence for formation of multimeric pores
    • Wimley, W. C., Selsted, M. E., and White, S. H. (1994) Interactions between human defensins and lipid bilayers: Evidence for formation of multimeric pores. Protein Sci. 3, 1362-1373.
    • (1994) Protein Sci , vol.3 , pp. 1362-1373
    • Wimley, W.C.1    Selsted, M.E.2    White, S.H.3
  • 9
    • 0031034840 scopus 로고    scopus 로고
    • Differential scanning microcalorimetry indicates that human defensin, HNP-2, interacts specifically with biomembrane mimetic systems
    • Lohner, K., Latal, A., Lehrer, R. I., and Ganz, T. (1997) Differential scanning microcalorimetry indicates that human defensin, HNP-2, interacts specifically with biomembrane mimetic systems. Biochemistry 36, 1525-1531.
    • (1997) Biochemistry , vol.36 , pp. 1525-1531
    • Lohner, K.1    Latal, A.2    Lehrer, R.I.3    Ganz, T.4
  • 10
    • 68849118093 scopus 로고    scopus 로고
    • Nes, I. F., Holo, H., Fimland, G., Hauge, H. H., and Nissen-Meyer, J. (2002) Unmodified peptide-bacteriocins (class II) produced by lactic acid bacteria. In Peptide Antibiotics: Discovery, Modes of Action and Application (Dutton, C., Haxell, M., McArthur, H., and Wax, R. G., Eds.) Marcel Dekker, Inc., New York.
    • Nes, I. F., Holo, H., Fimland, G., Hauge, H. H., and Nissen-Meyer, J. (2002) Unmodified peptide-bacteriocins (class II) produced by lactic acid bacteria. In Peptide Antibiotics: Discovery, Modes of Action and Application (Dutton, C., Haxell, M., McArthur, H., and Wax, R. G., Eds.) Marcel Dekker, Inc., New York.
  • 11
    • 28044472548 scopus 로고    scopus 로고
    • Pediocin-like antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: Biosynthesis, structure, and mode of action
    • Fimland, G., Johnsen, L., Dalhus, B., and Nissen-Meyer, J. (2005) Pediocin-like antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: Biosynthesis, structure, and mode of action. J. Pept. Sci. 11, 688-696.
    • (2005) J. Pept. Sci , vol.11 , pp. 688-696
    • Fimland, G.1    Johnsen, L.2    Dalhus, B.3    Nissen-Meyer, J.4
  • 12
    • 0029833708 scopus 로고    scopus 로고
    • New biologically active hybrid bacteriocins constructed by combining regions from various pediocin-like bacteriocins: The C-terminal region is important for determining specificity
    • Fimland, G., Blingsmo, O. R., Sletten, K., Jung, G., Nes, I. F., and Nissen-Meyer, J. (1996) New biologically active hybrid bacteriocins constructed by combining regions from various pediocin-like bacteriocins: The C-terminal region is important for determining specificity. Appl. Environ. Microbiol. 62, 3313-3318.
    • (1996) Appl. Environ. Microbiol , vol.62 , pp. 3313-3318
    • Fimland, G.1    Blingsmo, O.R.2    Sletten, K.3    Jung, G.4    Nes, I.F.5    Nissen-Meyer, J.6
  • 13
    • 0037199421 scopus 로고    scopus 로고
    • Mutational analysis of the role of tryptophan residues in an antimicrobial peptide
    • Fimland, G., Eijsink, V. G. H., and Nissen-Meyer, J. (2002) Mutational analysis of the role of tryptophan residues in an antimicrobial peptide. Biochemistry 41, 9508-9515.
    • (2002) Biochemistry , vol.41 , pp. 9508-9515
    • Fimland, G.1    Eijsink, V.G.H.2    Nissen-Meyer, J.3
  • 14
    • 0031934614 scopus 로고    scopus 로고
    • New types of clotting factors and defense molecules found in horseshoe crab hemolymph: Their structures and functions
    • Iwanaga, S., Kawabata, S., and Muta, T. (1998) New types of clotting factors and defense molecules found in horseshoe crab hemolymph: Their structures and functions. J. Biochem. 123, 1-15.
    • (1998) J. Biochem , vol.123 , pp. 1-15
    • Iwanaga, S.1    Kawabata, S.2    Muta, T.3
  • 15
    • 0036467504 scopus 로고    scopus 로고
    • The molecular basis of innate immunity in the horseshoe crab
    • Iwanaga, S. (2002) The molecular basis of innate immunity in the horseshoe crab. Curr. Opin. Immunol. 14, 87-95.
    • (2002) Curr. Opin. Immunol , vol.14 , pp. 87-95
    • Iwanaga, S.1
  • 16
    • 0025989172 scopus 로고
    • Morphology of the granular hemocytes of the Japanese horseshoe crab Tachypleus tridentatus and immunocytochemical localization of clotting factors and antimicrobial substances
    • Toh, Y., Mizutani, A., Tokunaga, F., Muta, T., and Iwanaga, S. (1991) Morphology of the granular hemocytes of the Japanese horseshoe crab Tachypleus tridentatus and immunocytochemical localization of clotting factors and antimicrobial substances. Cell Tissue Res. 266, 137-147.
    • (1991) Cell Tissue Res , vol.266 , pp. 137-147
    • Toh, Y.1    Mizutani, A.2    Tokunaga, F.3    Muta, T.4    Iwanaga, S.5
  • 17
    • 3843151565 scopus 로고    scopus 로고
    • Lipopolysaccharide-binding molecules: Transporters, blockers and sensors
    • Chaby, R. (2004) Lipopolysaccharide-binding molecules: Transporters, blockers and sensors. Cell. Mol. Life Sci. 61, 1697-1713.
    • (2004) Cell. Mol. Life Sci , vol.61 , pp. 1697-1713
    • Chaby, R.1
  • 18
    • 0029020955 scopus 로고
    • A novel big defensin identified in horseshoe crab hemocytes: Isolation, amino acid sequence, and antimicrobial activity
    • Saito, T., Kawabata, S., Shigenaga, T., Takayenoki, Y., Cho, J., Nakajima, H., Hirata, M., and Iwanaga, S. (1995) A novel big defensin identified in horseshoe crab hemocytes: Isolation, amino acid sequence, and antimicrobial activity. J. Biochem. 117, 1131-1137.
    • (1995) J. Biochem , vol.117 , pp. 1131-1137
    • Saito, T.1    Kawabata, S.2    Shigenaga, T.3    Takayenoki, Y.4    Cho, J.5    Nakajima, H.6    Hirata, M.7    Iwanaga, S.8
  • 20
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 22
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler, L., and Ernst, R. R. (1983) Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy. J. Magn. Reson. 53, 521-528.
    • (1983) J. Magn. Reson , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 23
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar, A., Ernst, R. R., and Wuthrich, K. (1980) A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 9, 1-6.
    • (1980) Biochem. Biophys. Res. Commun , vol.9 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wuthrich, K.3
  • 26
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 27
    • 68849110601 scopus 로고    scopus 로고
    • Goddard, T. D., and Kneller, D. G. (2005) Sparky 3 , University of California, San Franciso.
    • Goddard, T. D., and Kneller, D. G. (2005) Sparky 3 , University of California, San Franciso.
  • 28
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wuthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 29
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., Rullman, J. A., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullman, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 30
    • 33750071412 scopus 로고    scopus 로고
    • Sensitibity enhancement of multidimensional NMR experiments by paramagnetic relaxation effects
    • Cai, S., Seu, C., Kovacs, Z., Sherry, D., and Chen, Y. (2006) Sensitibity enhancement of multidimensional NMR experiments by paramagnetic relaxation effects. J. Am. Chem. Soc. 128, 13474-13478.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 13474-13478
    • Cai, S.1    Seu, C.2    Kovacs, Z.3    Sherry, D.4    Chen, Y.5
  • 31
    • 0034912658 scopus 로고    scopus 로고
    • Micellar systems as solvents in peptide and protein structure determination
    • Damberg, P., Jarvet, J., and Gräslund, A. (2001) Micellar systems as solvents in peptide and protein structure determination. Methods Enzymol. 339, 271-285.
    • (2001) Methods Enzymol , vol.339 , pp. 271-285
    • Damberg, P.1    Jarvet, J.2    Gräslund, A.3
  • 32
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C., and White, S. H. (1996) Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3, 842-848.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 33
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interface
    • White, S. H., and Wimley, W. C. (1998) Hydrophobic interactions of peptides with membrane interface. Biochim. Biophys. Acta 1376, 339-352.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 34
    • 0242488929 scopus 로고    scopus 로고
    • Translocons, thermodynamics, and the folding of membrane proteins
    • White, S. H. (2003) Translocons, thermodynamics, and the folding of membrane proteins. FEBS Lett. 555, 116-121.
    • (2003) FEBS Lett , vol.555 , pp. 116-121
    • White, S.H.1
  • 35
    • 15744401646 scopus 로고    scopus 로고
    • The C-termial domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C-terminal part of cognate immunity proteins and in determining the antimicrobial spectrum
    • Johnsen, L., Fimland, G., and Nissen-Meyer, J. (2005) The C-termial domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C-terminal part of cognate immunity proteins and in determining the antimicrobial spectrum. J. Biol. Chem. 280, 9243-9250.
    • (2005) J. Biol. Chem , vol.280 , pp. 9243-9250
    • Johnsen, L.1    Fimland, G.2    Nissen-Meyer, J.3
  • 36
    • 0032516737 scopus 로고    scopus 로고
    • A novel bacteriocin with a YGNGV motif from vegetable-associated Enterococcus mundtii: Full characterization and interaction with target organisms
    • Bennik, M. H. J., Vanloo, B., Brasseur, R., Gorris, L. G. M., and Smid, E. J. (1998) A novel bacteriocin with a YGNGV motif from vegetable-associated Enterococcus mundtii: Full characterization and interaction with target organisms. Biochim. Biophys. Acta 1373, 47-58.
    • (1998) Biochim. Biophys. Acta , vol.1373 , pp. 47-58
    • Bennik, M.H.J.1    Vanloo, B.2    Brasseur, R.3    Gorris, L.G.M.4    Smid, E.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.